Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

HS,(+/-)

Synonyms:

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Disease relevance of Heparan sulfate

We demonstrate that one mechanism through which EC-SOD inhibits lung inflammation and fibrosis in asbestosis is by protecting heparin/heparan sulfate from oxidative fragmentation [1].
Given this finding, mild, but clinically relevant, hyperlipidemias in human patients may be a result of alterations in heparan sulfate structure or possible genetic polymorphisms in the relevant biosynthetic genes [2].

Associations of Heparan sulfate with other chemical compounds

An arginine-rich peptide shows both heparan sulfate-dependent and -independent cellular uptake [3].
Heparin treatment of cultures induces many of the same biological effects as treatment with heparan sulfate, including elevated pERK levels in preBCR+ cells [4].
The heparan sulfate chains that do not bind antithrombin surprisingly exhibit an extremely high content in 3-O-sulfated glucosamine residues, which suggest that they may exhibit biological activities through interactions with other proteins [5].
Antagonizing heparan sulfate side chain formation with beta-xyloside or the addition of soluble heparin prevented ERK activation, in addition to reducing the expression of these proadhesive/contractile proteins [6].
The direct binding between integrins and heparin/heparan sulfate might explain why both heparan sulfate and alpha5beta1 integrin are required for the localization of endostatin in endothelial cell lipid rafts [7].

Gene context of Heparan sulfate

Loss of modified heparan sulphate in the GBM as a result of degradation by heparanase was confirmed by heparan sulphate staining of heparanase-treated normal kidney biopsy specimens [8].

References

Extracellular superoxide dismutase protects against matrix degradation of heparan sulfate in the lung. Kliment, C.R., Tobolewski, J.M., Manni, M.L., Tan, R.J., Enghild, J., Oury, T.D. Antioxid. Redox Signal. (2008) [Pubmed]
Heparan sulfate proteoglycans and triglyceride-rich lipoprotein metabolism. Bishop, J.R., Stanford, K.I., Esko, J.D. Curr. Opin. Lipidol. (2008) [Pubmed]
Guanidinylated neomycin delivers large, bioactive cargo into cells through a heparan sulfate-dependent pathway. Elson-Schwab, L., Garner, O.B., Schuksz, M., Crawford, B.E., Esko, J.D., Tor, Y. J. Biol. Chem. (2007) [Pubmed]
Heparan sulfate and heparin enhance ERK phosphorylation and mediate preBCR-dependent events during B lymphopoiesis. Milne, C.D., Corfe, S.A., Paige, C.J. J. Immunol. (2008) [Pubmed]
Human follicular fluid heparan sulfate contains abundant 3-O-sulfated chains with anticoagulant activity. de Agostini, A.I., Dong, J.C., de Vantéry Arrighi, C., Ramus, M.A., Dentand-Quadri, I., Thalmann, S., Ventura, P., Ibecheole, V., Monge, F., Fischer, A.M., HajMohammadi, S., Shworak, N.W., Zhang, L., Zhang, Z., Linhardt, R.J. J. Biol. Chem. (2008) [Pubmed]
Heparan sulfate-dependent ERK activation contributes to the overexpression of fibrotic proteins and enhanced contraction by scleroderma fibroblasts. Chen, Y., Leask, A., Abraham, D.J., Pala, D., Shiwen, X., Khan, K., Liu, S., Carter, D.E., Wilcox-Adelman, S., Goetinck, P., Denton, C.P., Black, C.M., Pitsillides, A.A., Sarraf, C.E., Eastwood, M. Arthritis Rheum. (2008) [Pubmed]
Molecular interplay between endostatin, integrins, and heparan sulfate. Faye, C., Moreau, C., Chautard, E., Jetne, R., Fukai, N., Ruggiero, F., Humphries, M.J., Olsen, B.R., Ricard-Blum, S. J. Biol. Chem. (2009) [Pubmed]
Heparanase induces a differential loss of heparan sulphate domains in overt diabetic nephropathy. Wijnhoven, T.J., van den Hoven, M.J., Ding, H., van Kuppevelt, T.H., van der Vlag, J., Berden, J.H., Prinz, R.A., Lewis, E.J., Schwartz, M., Xu, X. Diabetologia (2008) [Pubmed]

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